alexa Amino acid-anticodon binding specificity: rationale for a new class of therapeutic agent.
Oncology

Oncology

Journal of Carcinogenesis & Mutagenesis

Author(s): Melzer MS

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Abstract In this article a new class of anticancer and antiviral drugs is discussed. These new drugs consist of small di- and tri-peptides, designed to bind to single-stranded (ss) regions that are crucial for the expression of genes such as the c-myc oncogene in cancers and start sites (and other ss regions) of viral pathogenic genes. The components (i.e. the amino acids and the sequences they form) of these peptides could be dictated by the specific binding of amino acids to their ss anticodons in tRNA. Cancer cell viability depends on the continued overexpression of the c-myc oncogene, and thus this gene is a target of opportunity for anticancer agents. Sharply reducing the overexpression of c-myc leads to the death of cancer cells. To achieve this end the following rationale is suggested: crucial regions of the c-myc promoters (to which activating proteins must bind for expression to occur) are single stranded and thus strongly resemble the anticodon loop of tRNA. It was found that amino acids chemically bind to their cognate tRNA anticodons. Regarding the ss regions of c-myc as a series of adjacent 'anticodons', di- and tri-peptides are proposed to be aligned to their cognate 'anticodons' in the proper order. For example, if the ss region of a promoter is hypothetically TTT-GGG-CCC, the tripeptide Lys-Pro-Gly could be expected to bind to it and deny access of the promoter to all activating proteins, thereby blocking c-myc expression and all the cancers dependent on such overexpression. Similarly, it is reported that in the initial phase of gene expression the start sites of the genes are single stranded (before and after and spanning the start site). Thus, invoking the amino acid cognate anticodon binding specificity (ACABS) principle as described above, a series of small peptides are suggested that could span the start sites of pathogenic viral genes (e.g. the oris region of herpes simplex virus (HSV)) to deny access of the gene to the transcription elements. This would inactivate the toxic effect of the virus and thereby constitute a promising approach to antiviral therapy, where the start sites (or other ss regions of pathogenic genes) have been sequenced. The ACABS principle (for peptide-nucleic-acid interaction) enables us to focus on probable effective small peptides rather than having to screen a large number of randomly chosen small peptides to find probable anticancer and antiviral therapeutic agents. Copyright © 2011 Elsevier Ltd. All rights reserved. This article was published in Drug Discov Today and referenced in Journal of Carcinogenesis & Mutagenesis

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